TY  - JOUR
A1  - Himmel, Mirko
A1  - VanderVen, Peter F. M.
A1  - Stöcklein, Walter F. M.
A1  - Fürst, Dieter Oswald
T1  - The limits of promiscuity : isoform-specific dimerization of filamins
Y1  - 2003
ER  - 
TY  - JOUR
A1  - Obermann, Wolfgang
A1  - Gautel, Mathias
A1  - Steiner, F.
A1  - VanDerVen, Peter F. M.
A1  - Weber, Klaus
A1  - Fürst, Dieter Oswald
T1  - The structure of the sarcomeric M band : localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Obermann, Wolfgang
A1  - VanDerVen, Peter F. M
A1  - Steiner, F.
A1  - Weber, Klaus
A1  - Fürst, Dieter Oswald
T1  - Mapping of a myosin binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M-band
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Vorgerd, M.
A1  - vanderVen, Peter F. M.
A1  - Bruchertseifer, V.
A1  - Lowe, T.
A1  - Kley, R. A.
A1  - Schröder, Rolf
A1  - Lochmuller, H.
A1  - Himmel, Mirko
A1  - Koehler, K.
A1  - Fürst, Dieter Oswald
A1  - Huebner, A.
T1  - A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy
N2  - Myofibrillar myopathy (MFM) is a human disease that is characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. In an extended German pedigree with a novel form of MFM characterized by clinical features of a limb-girdle myopathy and morphological features of MFM, we identified a cosegregating, heterozygous nonsense mutation (8130G -> A; W2710X) in the filamin c gene ( FLNC) on chromosome 7q32.1. The mutation is the first found in FLNC and is localized in the dimerization domain of filamin c. Functional studies showed that, in the truncated mutant protein, this domain has a disturbed secondary structure that leads to the inability to dimerize properly. As a consequence of this malfunction, the muscle fibers of our patients display massive cytoplasmic aggregates containing filamin c and several Z-disk-associated and sarcolemmal proteins
Y1  - 2005
SN  - 0002-9297
ER  - 
TY  - JOUR
A1  - Kleuser, U.
A1  - Stöcklein, Walter F. M.
A1  - Pieper-Fürst, U.
A1  - Scheller, Frieder W.
T1  - Partikelverstärkte Oberflächenplasmonresonanz für die Quantifizierung von Matrix Metalloproteinase-2
Y1  - 2004
ER  - 
TY  - JOUR
A1  - Gehmlich, Katja
A1  - Geier, C.
A1  - Osterziel, Karl Joseph
A1  - VanderVen, Peter F. M.
A1  - Fürst, Dieter Oswald
T1  - Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy
N2  - Previous work has shown that mutations in muscle LIM protein (MLP) can cause hypertrophic cardiomyopathy (HCM). In order to gain an insight into the molecular basis of the disease phenotype, we analysed the binding characteristics of wild-type MLP and of the (C58G) mutant MLP that causes hypertrophic cardiomyopathy. We show that MLP can form a ternary complex with two of its previously documented myofibrillar ligand proteins, N-RAP and alpha-actinin, which indicates the presence of distinct, non-overlapping binding sites. Our data also show that, in comparison to wild-type MLP, the capacity of the mutated MLP protein to bind both N-RAP and alpha-actinin is significantly decreased. In addition, this single point mutation prevents zinc coordination and proper folding of the second zinc-finger in the first LIM domain, which consequently renders the protein less stable and more susceptible to proteolysis. The molecular basis for HCM-causing mutations in the MLP gene might therefore be an alteration in the equilibrium of interactions of the ternary complex MLP-N-RAP-alpha-actinin. This assumption is supported by the previous observation that in the pathological situation accompanied by MLP down regulation, cardiomyocytes try to compensate for the decreased stability of MLP protein by increasing the expression of its ligand N-RAP, which might finally result in the development of myocyte disarray that is characteristic of this disease
Y1  - 2004
SN  - 0302-766X
ER  - 
TY  - JOUR
A1  - Pieper-Fürst, U.
A1  - Kleuser, U.
A1  - Stöcklein, Walter F. M.
A1  - Warsinke, Axel
A1  - Scheller, Frieder W.
T1  - Detection of subicomolar concentrations of human matrix metalloproteinase-2 by an optical biosensor
N2  - We describe in this paper the development of a one-step sandwich assay for the highly sensitive and fast detection of human matrix metalloproteinase (MMP)-2 (EC 3.4.24.24), using surface plasmon resonance (SPR). For the assay, two ligands were selected: monoclonal anti-MMP-2 antibody Ab-2 and the tissue inhibitor of metalloproteinases (TIMP)-2. They were chosen on the basis of (1) their affinities to MMP-2, (2) the efficiency of immobilization to the sensor chip, (3) the efficiency of adsorption to colloidal gold, and (4) the stability of these protein-coated gold particles. The assay included mixing of MMP-2 with antibody Ab-2 adsorbed to colloidal gold with a diameter of about 20 rim and injection into the flowcell of the SPR instrument containing immobilized TIMP-2. By using colloidal gold particles an amplification factor of 114 and a detection limit of 0.5 pM for MMP-2 were obtained. The precision of the assay was high even at low analyte concentrations, the standard deviation being 8.3% for five determinations of 1 pM MMP- 2. No significant binding was observed with the structurally related MMP-9. The assay is far more sensitive and faster than commonly used methods for MMP-2 detection. As TIMP-bound MMP-2 is not detected by this method, the assay can be applied for measuring free MMP-2, reflecting the imbalance of free and inhibitor-bound enzyme in various pathological situations. (C) 2004 Elsevier Inc. All rights reserved
Y1  - 2004
ER  - 
TY  - JOUR
A1  - Pacholsky, Dirk
A1  - Vakeel, Padmanabhan
A1  - Himmel, Mirko
A1  - Lowe, T.
A1  - Stradal, T.
A1  - Rottner, K.
A1  - Fürst, Dieter Oswald
A1  - vanderVen, Peter F. M.
T1  - Xin repeats define a novel actin-binding motif
N2  - Xin is a protein that is expressed during early developmental stages of cardiac and skeletal muscles. Immunolocalization studies indicated a peripheral localization in embryonic mouse heart, where Xin localizes with beta- catenin and N-cadherin. In adult tissues, Xin is found primarily in the intercalated discs of cardiomyocytes and the myotendinous junctions of skeletal muscle cells, both specialized attachment sites of the myofibrillar ends to the sarcolemma. A large part of the Xin protein consists of unique 16 amino acid repeats with unknown function. We have investigated the characteristics of the Xin repeats by transfection experiments and actin-binding assays and ascertained that, upon expression in cultured cells, these repeats bind to and stabilize the actin-based cytoskeleton. In vitro co- sedimentation assays with skeletal muscle actin indicated that they not only directly bind actin filaments, but also have the capability of arranging microfilaments into networks that sediment upon low-speed centrifugation. Very similar repeats were also found in Xin-repeat protein 2' (XIRP2), a novel protein that seems to be expressed mainly in striated muscles. Human XIRP2 contains 28 Xin repeats with properties identical to those of Xin. We conclude that the Xin repeats define a novel, repetitive actin-binding motif present in at least two different muscle proteins. These Xin- repeat proteins therefore constitute the first two members of a novel family of actin-binding proteins
Y1  - 2004
SN  - 0021-9533
ER  - 
TY  - JOUR
A1  - Martinez-Chicharro, M.
A1  - Torrejon, J. M.
A1  - Oskinova, Lida
A1  - Furst, F.
A1  - Postnov, K.
A1  - Rodes-Roca, J. J.
A1  - Hainich, Rainer
A1  - Bodaghee, A.
T1  - Evidence of Compton cooling during an X-ray flare supports a neutron star nature of the compact object in 4U1700-37
JF  - Monthly notices of the Royal Astronomical Society
N2  - Based on new Chandra X-ray telescope data, we present empirical evidence of plasma Compton cooling during a flare in the non-pulsating massive X-ray binary 4U1700-37. This behaviour might be explained by quasi-spherical accretion on to a slowly rotating magnetized neutron star (NS). In quiescence, the NS in 4U1700-37 is surrounded by a hot radiatively cooling shell. Its presence is supported by the detection of mHz quasi-periodic oscillations likely produced by its convection cells. The high plasma temperature and the relatively low X-ray luminosity observed during the quiescence, point to a small emitting area similar to 1 km, compatible with a hotspot on an NS surface. The sudden transition from a radiative to a significantly more efficient Compton cooling regime triggers an episode of enhanced accretion resulting in a flare. During the flare, the plasma temperature drops quickly. The predicted luminosity for such transitions, similar to 3 x 10(35) erg s(-1), is very close to the luminosity of 4U1700-37 during quiescence. The transition may be caused by the accretion of a clump in the stellar wind of the donor star. Thus, a magnetized NS nature of the compact object is strongly favoured.
KW  - stars: individual: 4U1700-37
KW  - V*V884 Sco
KW  - X-rays: binaries
Y1  - 2017
U6  - https://doi.org/10.1093/mnrasl/slx165
SN  - 0035-8711
SN  - 1365-2966
VL  - 473
IS  - 1
SP  - L74
EP  - L78
PB  - Oxford Univ. Press
CY  - Oxford
ER  - 
TY  - JOUR
A1  - VanDerLoop, Frank T. L.
A1  - VanDerVen, Peter F. M
A1  - Fürst, Dieter Oswald
A1  - Gautel, Mathias
A1  - VanEys, Guillaume
A1  - Ramaekers, Frans C. S.
T1  - Integration of titin into the sarcomeres of cultured differentiating human skeletal muscle cells
Y1  - 1996
ER  - 
TY  - JOUR
A1  - VanDerVen, Peter F. M
A1  - Obermann, Wolfgang
A1  - Weber, Klaus
A1  - Fürst, Dieter Oswald
T1  - Myomesin, M-protein and the structure of the sarcomeric M-band
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Mayans, Olga
A1  - VanDerVen, Peter F. M
A1  - Wilmanns, Matthias
A1  - Mues, Alexander
A1  - Young, Paul
A1  - Fürst, Dieter Oswald
A1  - Wilmanns, Matthias
A1  - Gautel, Mathias
T1  - The structural basis of the activation of the serine kinase domain of the giant muscle protein titin during myofibrillogenesis
Y1  - 1998
ER  - 
TY  - JOUR
A1  - VanDerVen, Peter F. M
A1  - Fürst, Dieter Oswald
T1  - Expression of sarcomeric proteins and assembly of myofibrils in the putative myofibroblast cell line BHK-21/C13
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Speel, Ernst J. M.
A1  - VanDerVen, Peter F. M.
A1  - Albrechts, Jozefa C. M.
A1  - Hopman, Anton H. N.
A1  - Fürst, Dieter Oswald
T1  - Chromosomal assignment of the human myomesin gene
Y1  - 1998
ER  - 
TY  - JOUR
A1  - VanDerVen, Peter F. M
A1  - Fürst, Dieter Oswald
T1  - Assembly of titin, myomesin and M-protein into the sarcomeric M-band in differentiating human skeletal muscle cells in vitro
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Steiner, F.
A1  - Weber, Klaus
A1  - Fürst, Dieter Oswald
T1  - Structure and expression of the gene encoding murine M-protein, a sarcomere-specific member of the immunoglobulin superfamily
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Mues, Alexander
A1  - VanDerVen, Peter F. M
A1  - Young, Paul
A1  - Fürst, Dieter Oswald
A1  - Gautel, Mathias
T1  - Two immunoglobulin-like domains of the Z-disk portion of titin interact in a conformation-dependent way with telethonin
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Speel, Ernst J. M.
A1  - VanDerVen, Peter F. M.
A1  - Albrechts, Jozefa C. M.
A1  - Ramaekers, Frans C. S.
A1  - Fürst, Dieter Oswald
A1  - Hopman, Anton H. N.
T1  - Assignment of the human gene for the sarcomeric M-band protein myomesin (MYOM1) to 18p11.31-p11.32
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Schröder, Rolf
A1  - VanDerVen, Peter F. M.
A1  - Warlo, Irene
A1  - Schumann, H.
A1  - Fürst, Dieter Oswald
A1  - Blümke, Ingmar
A1  - Goebel, Hans H.
A1  - Schmidt, M. C.
A1  - Hatzfeld, Mechthild
T1  - A member of the armadillo multigene family, is a constituent of sarcomeric I-bands in human skeletal muscle
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Schröder, Rolf
A1  - Fürst, Dieter Oswald
A1  - Klasen, Christian
A1  - Reiman, Jens
A1  - Herrmann, Harald
A1  - VanDerVen, Peter F. M.
T1  - The association of plectin with Z-discs is a prerequisite for the formation of the intermyofibrillar desmin cytoskeleton
Y1  - 2000
ER  -